Information on EC 1.3.3.6 - acyl-CoA oxidase

New: Word Map on EC 1.3.3.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.3.3.6
-
RECOMMENDED NAME
GeneOntology No.
acyl-CoA oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
anti-elimination of pro-2R and pro-3R hydrogens of acyl-CoA
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
anti-elimination of pro-2R and pro-3R hydrogens of acyl-CoA
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
inducible by growth on di-(2-ethylhexyl)phthalate
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
structural analysis of enzyme complexed with 3-ketoacyl-CoA substrate analogues
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
acts on CoA derivatives of fatty acids with chain length from 8 to 18
-
-
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
stereochemistry of the reaction
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
genetic regulation
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
mechanism, substrate binding site, and active site structure
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
10-cis-heptadecenoyl-CoA degradation (yeast)
-
-
10-trans-heptadecenoyl-CoA degradation (reductase-dependent, yeast)
-
-
6-gingerol analog biosynthesis
-
-
9-cis, 11-trans-octadecadienoyl-CoA degradation (isomerase-dependent, yeast)
-
-
alpha-Linolenic acid metabolism
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of unsaturated fatty acids
-
-
docosahexaenoate biosynthesis III (mammals)
-
-
fatty acid beta-oxidation (peroxisome, yeast)
-
-
fatty acid beta-oxidation II (peroxisome)
-
-
fatty acid beta-oxidation V (unsaturated, odd number, di-isomerase-dependent)
-
-
fatty acid beta-oxidation VI (peroxisome)
-
-
Fatty acid degradation
-
-
jasmonic acid biosynthesis
-
-
lipid metabolism
-
-
Metabolic pathways
-
-
methyl ketone biosynthesis
-
-
oleate beta-oxidation (isomerase-dependent, yeast)
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:oxygen 2-oxidoreductase
A flavoprotein (FAD). Acts on CoA derivatives of fatty acids with chain lengths from 8 to 18.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3alpha,7alpha, 12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase
-
-
-
-
acyl coenzyme A oxidase
-
-
-
-
Acyl-CoA oxidase
-
-
-
-
AOX
-
-
-
-
BRCACox
-
-
-
-
fatty acyl-CoA oxidase
-
-
-
-
fatty acyl-coenzyme A oxidase
-
-
-
-
oxidase, acyl-coenzyme A
-
-
-
-
Peroxisomal fatty acyl-CoA oxidase
-
-
-
-
Pristanoyl-CoA oxidase
-
-
-
-
THCA-CoA oxidase
-
-
-
-
THCCox
-
-
-
-
Trihydroxycoprostanoyl-CoA oxidase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
61116-22-1
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Col-0 accession
-
-
Manually annotated by BRENDA team
isoforms AtACX1, AtACX2, and AtACX3
-
-
Manually annotated by BRENDA team
isoforms AtACX1, AtACX2, AtACX3, and AtSACX
SwissProt
Manually annotated by BRENDA team
six ACX genes, acx1-acx6. ACX6 is not expressed
-
-
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
six ACX genes, acx1-acx6. ACX6 is not expressed
-
-
Manually annotated by BRENDA team
strain 2-4-1
SwissProt
Manually annotated by BRENDA team
Arthrobacter sp. 02.04.2001
strain 2-4-1
SwissProt
Manually annotated by BRENDA team
strain NBRC 12140
SwissProt
Manually annotated by BRENDA team
Arthrobacter ureafaciens NBRC 12140
strain NBRC 12140
SwissProt
Manually annotated by BRENDA team
strain GHA
-
-
Manually annotated by BRENDA team
Beauveria bassiana GHA
strain GHA
-
-
Manually annotated by BRENDA team
Candida sp.
-
-
-
Manually annotated by BRENDA team
pK 233, inducible by growth on alkanes
-
-
Manually annotated by BRENDA team
cucumber
-
-
Manually annotated by BRENDA team
Cucurbita sp.
pumpkin
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
ACOX1a and ACOX1b isoforms are encoded by a single gene
-
-
Manually annotated by BRENDA team
C57BL/6J mice
-
-
Manually annotated by BRENDA team
no activity in Sporidiobolus pararoseus
strain CBS484
-
-
Manually annotated by BRENDA team
no activity in Sporidiobolus pararoseus CBS484
strain CBS484
-
-
Manually annotated by BRENDA team
3 forms: 1. inducible fatty acyl-CoA oxidase, 2. noninducible fatty acyl-CoA oxidase, 3. noninducible trihydroxycoprostanoyl-CoA oxidase
-
-
Manually annotated by BRENDA team
inducible by growth on di-(2-ethylhexyl)phthalate
-
-
Manually annotated by BRENDA team
two isoforms: ACO-I, ACO-II
-
-
Manually annotated by BRENDA team
oleate-inducible
-
-
Manually annotated by BRENDA team
strain CBS5001
-
-
Manually annotated by BRENDA team
Sporidiobolus ruineniae CBS5001
strain CBS5001
-
-
Manually annotated by BRENDA team
from Lophius americanus
-
-
Manually annotated by BRENDA team
mung bean
-
-
Manually annotated by BRENDA team
i.e. Yarrowia lipolytica; isoform AOX3
-
-
Manually annotated by BRENDA team
six acyl-CoA oxidase isoenzymes encoded by genes POX1-POX6
-
-
Manually annotated by BRENDA team
strain W29 (ATCC 20460)
-
-
Manually annotated by BRENDA team
Yarrowia lipolytica W29
six acyl-CoA oxidase isoenzymes encoded by genes POX1-POX6
-
-
Manually annotated by BRENDA team
Yarrowia lipolytica W29
strain W29 (ATCC 20460)
-
-
Manually annotated by BRENDA team
medium-chain specific isoform, MCOX, and short-chain specific isoform, SCOX
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
deletion of gene aoxA leads to reduced growth on long chain fatty acids, but growth is not abolished by this mutation
malfunction
-
the acx3acx4Col and acx1acx3acx4Col mutants are viable, enzyme activity in these mutants is significantly reduced on a range of substrates compared to the wild-type. Reducing ACX4 expression in several Arabidopsis backgrounds shows a split response, suggesting that the ACX4 gene and/or protein functions differently in Arabidopsis accessions, phenotypes, detailed overview. ACX2 levels are increased in acx1acx3acx4Col compared to Col-0 wild-type samples
malfunction
Arabidopsis thaliana Col-0
-
the acx3acx4Col and acx1acx3acx4Col mutants are viable, enzyme activity in these mutants is significantly reduced on a range of substrates compared to the wild-type. Reducing ACX4 expression in several Arabidopsis backgrounds shows a split response, suggesting that the ACX4 gene and/or protein functions differently in Arabidopsis accessions, phenotypes, detailed overview. ACX2 levels are increased in acx1acx3acx4Col compared to Col-0 wild-type samples
-
metabolism
-
ACOX1 is the first and rate-limiting enzyme of the peroxisomal beta-oxidation pathway
metabolism
-
SCOX is the first enzyme of the peroxisomal beta-oxidation system and is involved in the oxidation of various fatty acids including very-long-chain fatty acids, long-chain dicarboxylic acids and polyunsaturated fatty acids, but not branched-chain fatty acids such as pristanic acid and the C27-bile acid intermediates
metabolism
-
the enzyme is involved in the peroxisomal beta-oxidation pathway
metabolism
-
the isozymes are involved in the beta-oxidation in peroxisomes. Aox3p function is responsible for 90% and 75% of the total polyhydroxyalkanoate produced from either C9:0 or C13:0 fatty acid, respectively, whereas Aox5p encodes the main Aox involved in the biosynthesis of 70% of polyhydroxyalkanoate from C9:0 fatty acid. Other Aox isozymes, such as Aox1p, Aox2p, Aox4p and Aox6p, play no significant role in PHA biosynthesis, independent of the chain length of the fatty acid used, leaky-hose pipe beta-oxidation cycle model in Yarrowia lipolytica, overview
physiological function
-
involved in fatty acid oxidation, essential energy generation
physiological function
-
ACOX1b controls the spontaneous hepatic peroxisome proliferation
metabolism
Yarrowia lipolytica W29
-
the isozymes are involved in the beta-oxidation in peroxisomes. Aox3p function is responsible for 90% and 75% of the total polyhydroxyalkanoate produced from either C9:0 or C13:0 fatty acid, respectively, whereas Aox5p encodes the main Aox involved in the biosynthesis of 70% of polyhydroxyalkanoate from C9:0 fatty acid. Other Aox isozymes, such as Aox1p, Aox2p, Aox4p and Aox6p, play no significant role in PHA biosynthesis, independent of the chain length of the fatty acid used, leaky-hose pipe beta-oxidation cycle model in Yarrowia lipolytica, overview
-
additional information
-
adult peroxisomal acyl-coenzyme A oxidase deficiency, formerly also called pseudoneonatal adrenoleucodystrophy, is a disorder of peroxisomal fatty acid oxidation with a severe presentation with cerebellar and brainstem atrophy, phenotype, overview. Accumulation of very-long-chain fatty acids is the only diagnostic marker for SCOX deficiency
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,16-hexadecadioyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
16-hydroxy-palmitoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
2-oxoheptadecyldethio-CoA + O2
?
show the reaction diagram
-
-
-
-
?
4,8,12-trimethyl-tridecanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
4-methyl-nonanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
6-phenyl-6-phenyl-hexanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
O65201, P0CZ23
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
O65201, O65202, P0CZ23, Q96329, Q9ZQP2
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
3'-phosphate on the ribose ring and the structure of the adenine moiety are essential for substrate recognition, specificity is relatively low with respect to the structure of the pantric acid moiety
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
isoform ACO-I prefers short-chain acyl-CoA substrates, isoform ACO-II prefers long-chain acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
isoform SCOX prefers C4-C8 substrates, isoform MCOX prefers C10-C14 substrates
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
anti-elimination of pro-2R and pro-3R hydrogens of acyl-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
specificity: C4-C20 acyl-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
enzyme acts selectively on fatty acyl-CoA with 16 or 18 carbon atoms, cis-9-unsaturated esters with a C16 or C18 acyl moiety being converted with higher rate than saturated or polyunsaturated fatty acyl-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
chain-length specificity changes with acyl-CoA concentration used
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
highly specific for short-chain fatty acids
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
most active towards C12-C18 acyl-CoA, C20 and C22 acyl-CoA also oxidized, C4 and C6 acyl-CoA hardly oxidized
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
both isoforms ACX1.1 and 1.2 show similar broad substrate specificities
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
preference for long-chain acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
Cucurbita sp.
-
preference for long-chain acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
AtACX1 is medium-chain specific, AtACX2 is medium- to long-chain specific
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
C4-C18 monocarboxylic acid-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
C8-C18 acyl CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
C8-C18 acyl CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
C8-C18 acyl CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
C6-C16 dicarboxylic-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
medium-chain-length specific
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
long- and short-chain acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
P0CZ23
AtACX3 is medium-chain-specific
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
AtACX3 is medium-chain-specific
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
P0CZ23
AtACX1 is medium- to long-chain specific, AtSACXis strictly short-chain specific
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
AtACX1 is medium- to long-chain specific, AtSACXis strictly short-chain specific
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
preference for C12-C18 acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
P0CZ23
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
Cucurbita sp.
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
CoA derivatives of fatty acids with chain length from 8 to 18, first reaction of peroxisomal beta-oxidation, rate limiting for this process
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
CoA derivatives of fatty acids with chain length from 8 to 18, first reaction of peroxisomal beta-oxidation, rate limiting for this process
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in lignin degradative system
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
beta-oxidation of dicarboxylic acid-CoAs in rat liver is carried out exclusively in peroxisomes
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
significance in metabolism of alkanes of Candida tropicalis
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
key enzyme of beta-oxidation. A basal level of long chain ACX is always present along the barley life cycle, while a higher level of expression is typical of actively growing tissues such as germinating embryos, ovary before anthesis, developing embryos, shoots and root apexes. The enzyme plays a role not only during oil reserve mobilization, but also in plant growth and metabolism
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
Yarrowia lipolytica W29
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
Sporidiobolus ruineniae CBS5001
-
-
-
-
?
acyl-CoA + O2
trans-2-enoyl-CoA + H2O2
show the reaction diagram
-
assay at 25C
-
-
ir
arachidoyl-CoA + O2
2-trans-eicosenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
behenoyl-CoA + O2
2-trans-docosenoyl-CoA + H2O2
show the reaction diagram
Beauveria bassiana, Beauveria bassiana GHA
-
-
-
-
?
butyryl-CoA + O2
trans-2-butenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
butyryl-CoA + O2
trans-2-butenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
cis-3-decenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
cis-3-hexenoyl-CoA + O2
?
show the reaction diagram
-
best substrate for the isomerase activity of the enzyme
-
-
?
cis-3-octenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
dec-4-cis-enoyl-CoA + O2
2-trans-4-cis-decadienoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
dec-4-cis-enoyl-CoA + O2
2-trans-4-cis-decadienoyl-CoA + H2O2
show the reaction diagram
-
-
-
?
dec-4-trans-enoyl-CoA + O2
2-trans-4-trans-decadienoyl-CoA + H2O2
show the reaction diagram
-
-
-
?
decanoyl-CoA + O2
trans-2-decenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
decanoyl-CoA + O2
trans-2-decenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
-
decanoyl-CoA + O2
trans-2-decenoyl-CoA + H2O2
show the reaction diagram
O74935
-
-
-
?
decanoyl-CoA + O2
trans-2-decenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
dicarboxylic acid-CoAs with 6-16 carbon atoms + O2
?
show the reaction diagram
-
-
-
-
?
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
show the reaction diagram
O74935
-
-
-
?
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
show the reaction diagram
P0CZ23
AtACX3 and AtACX1 show preference for
-
-
?
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
show the reaction diagram
O65201, O65202, P0CZ23, Q96329, Q9ZQP2
preferred substrate of ACX3
-
-
?
eicosapentaenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
furylpropionyl-CoA + O2
furylacryloyl-CoA + H2O2
show the reaction diagram
-
also oxidizes aromatic/heterocyclic ring-substituted chromogenic substrates
-
?
hexadecanedioyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
hexadecanedioyl-CoA + O2
?
show the reaction diagram
O74935
-
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
-
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
show the reaction diagram
-
recombinant enzyme
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
show the reaction diagram
P0CZ23
AtSACX shows preference for
-
-
?
indole-3-butyric acid-CoA + O2
?
show the reaction diagram
-
-
-
-
?
jasmonic acid-CoA + O2
?
show the reaction diagram
O65201, O65202, P0CZ23, Q96329, Q9ZQP2
preferred substrate of ACX1
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
show the reaction diagram
-
low activity
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
show the reaction diagram
P07872
binding mode of C12-fatty acid suggests that the active site does not close upon substrate binding, but remains spacious during the entire catalytic process, the oxygen accessibility in the oxidative half-reaction thereby being maintained
-
-
?
leuko-dichlorofluorescein + O2
?
show the reaction diagram
-
-
-
-
?
lignoceroyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
lignoceroyl-CoA + O2
?
show the reaction diagram
Beauveria bassiana, Beauveria bassiana GHA
-
-
-
-
?
linoleoyl-CoA + O2
2-trans-9-trans-12-trans-octadecatrienoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
O74935
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
Q33DR0
highest activity
-
-
ir
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
-
AtACX1
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
Q33DR0
maximum activity
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
O65201, O65202, P0CZ23, Q96329, Q9ZQP2
preferred substrate of ACX1
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
Arthrobacter ureafaciens NBRC 12140
Q33DR0
highest activity
-
-
ir
nonanoyl-CoA + O2
trans-2-nonenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
octadecanoyl-CoA + O2
?
show the reaction diagram
O65201, O65202, P0CZ23, Q96329, Q9ZQP2
preferred substrate of ACX2
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
-
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + O2
2-trans-9-trans-octadecendienoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + O2
2-trans-9-trans-octadecendienoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + O2
2-trans-9-trans-octadecendienoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
Q8HYL8
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
Q33DR0
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
Q33DR0
-
-
-
ir
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
Beauveria bassiana GHA
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
Arthrobacter ureafaciens NBRC 12140
Q33DR0
-
-
-
?, ir
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
show the reaction diagram
-
isozyme ACOX1b shows higher activity than isozyme ACOX1a
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
AtACX2
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
Beauveria bassiana GHA
-
-
-
-
?
trans-3-decenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
trans-3-hexenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
trans-3-octenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
trihydroxycoprostanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
linoleoyl-CoA + O2
2-trans-9-trans-12-trans-octadecatrienoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
structural and functional comparison of isoforms with each other and enzymes from other species, regulatory aspects
-
-
-
additional information
?
-
-
Aox2p expression regulates the size of cellular triacylglycerol pools and the size and number of intracellular lipid bodies in which these gatty acids accumulate
-
-
-
additional information
?
-
-
Eucalyptus terpenes elevate hepatic AOX expression in possum
-
-
-
additional information
?
-
-
key enzyme for the beta-oxidation of fatty acids
-
-
-
additional information
?
-
Q8HYL8
rate-limiting enzyme of the peroxisomal beta-oxidation spiral
-
-
-
additional information
?
-
O74935
no activity with hexadecanoyl-CoA and 3-methylheptadecanoyl-CoA
-
-
-
additional information
?
-
Q33DR0
high activity toward acyl-CoAs with a chain length of C12-C18, inactive with short chain acyl-CoAs with a chain length of C4 and C6
-
-
-
additional information
?
-
Q33DR0
exhibits high activity towards acyl-CoAs with chain lenghths of C12-C18
-
-
-
additional information
?
-
Arabidopsis thaliana, Arabidopsis thaliana Col-0
-
each ACX enzyme acts on specific chain-length targets, but in a partially overlapping manner, indicating a degree of functional redundancy
-
-
-
additional information
?
-
Arthrobacter ureafaciens NBRC 12140
Q33DR0
high activity toward acyl-CoAs with a chain length of C12-C18, inactive with short chain acyl-CoAs with a chain length of C4 and C6, exhibits high activity towards acyl-CoAs with chain lenghths of C12-C18
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
P0CZ23
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
Cucurbita sp.
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
CoA derivatives of fatty acids with chain length from 8 to 18, first reaction of peroxisomal beta-oxidation, rate limiting for this process
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
CoA derivatives of fatty acids with chain length from 8 to 18, first reaction of peroxisomal beta-oxidation, rate limiting for this process
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in lignin degradative system
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
beta-oxidation of dicarboxylic acid-CoAs in rat liver is carried out exclusively in peroxisomes
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
significance in metabolism of alkanes of Candida tropicalis
-
-
?
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
key enzyme of beta-oxidation. A basal level of long chain ACX is always present along the barley life cycle, while a higher level of expression is typical of actively growing tissues such as germinating embryos, ovary before anthesis, developing embryos, shoots and root apexes. The enzyme plays a role not only during oil reserve mobilization, but also in plant growth and metabolism
-
-
?
additional information
?
-
-
Aox2p expression regulates the size of cellular triacylglycerol pools and the size and number of intracellular lipid bodies in which these gatty acids accumulate
-
-
-
additional information
?
-
-
Eucalyptus terpenes elevate hepatic AOX expression in possum
-
-
-
additional information
?
-
-
key enzyme for the beta-oxidation of fatty acids
-
-
-
additional information
?
-
Q8HYL8
rate-limiting enzyme of the peroxisomal beta-oxidation spiral
-
-
-
additional information
?
-
Arabidopsis thaliana, Arabidopsis thaliana Col-0
-
each ACX enzyme acts on specific chain-length targets, but in a partially overlapping manner, indicating a degree of functional redundancy
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
flavoprotein
FAD
-
1.22 mol per mol of enzyme; flavoprotein; prosthetic group
FAD
-
flavoprotein; flavoprotein with noncovalently bound FAD
FAD
-
flavoprotein with noncovalently bound FAD
FAD
-
8 mol FAD per mol of enzyme, 1 mol FAD per mol of subunit; flavoprotein
FAD
-
tightly bound FAD, 4 mol per mol of enzyme octamer
FAD
-
flavoprotein
FAD
-
both subunits are involved in FAD-binding
FAD
-
flavoprotein with noncovalently bound FAD
FAD
-
required for the isomerase activity of the enzyme
FAD
Q33DR1
-
FAD
Q33DR0
flavoenzyme with 1 mol FAD per subunit; one molecule of non-covalently bound FAD per subunit as a prosthetic group
FAD
Candida sp.
-
-
FAD
Q4QRE2
;
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-bromopalmitic acid
-
-
2-Bromopalmitoyl-CoA
-
-
2-tetradecylglycidic acid
-
-
3,4-pentadienoyl-CoA
-
rapid, irreversible
3-ketoacyl-CoA substrate analogues
-
complex formation with anionic forms of 3-ketoacyl-CoA
3-ketohexadecanoyl-CoA
-
-
3-octynoyl-CoA
-
irreversible
5,5'-dithiobis(2-nitro-benzoic acid)
-
inactivates by modification of sulfhydryl groups and loss of FAD
acetyl-CoA
-
competitive inhibition
antimycin A
-
-
antimycin A
-
with addition of rotenone
C16-C18 fatty acyl-CoA
-
at fairly low concentrations
Detergents
-
inactiviation via dissociation of subunits
Detergents
-
no inhibition with Triton-X 100
FMN
-
uncompetitive inhibition
indole-3-butyric acid
-
inhibits root elongation
N-ethylmaleimide
Q33DR1
shows less than 10% activity in the presence of 10 mM at 37C for 4 h
N-ethylmaleimide
Q33DR0
ACO retains more than 60% of the initial activity in the presence of 10 mM N-ethylmaleimide, at 37C for 4 h; purified enzyme retains more than 60% activity in the presence of 10 mM at 37C for 4 h, while other commercially available ACOs show only less than 10% activities after the same treatment
N-ethylmaleimide
Candida sp.
-
shows less than 10% activity in the presence of 10 mM at 37 C for 4 h
oct-2-en-4-ynoyl-CoA
-
irreversible inactivation, pH dependent, higher under basic condition
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
slight inhibition
Phenol
-
high concentration, magnitude of inhibition depends on the nature of the acyl-CoA substrate
Phenylmethylsulfonylfluoride
-
slight inhibition
Mercuric acetate
-
-
additional information
-
glutathione protects against inhibition with sulfhydryl reagents
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-Amino-1,2,4-triazole
-
enhances acyl-CoA oxidation, avoids H2O2 consumption by endogenous catalase
alpha-linolenic acid-rich perilla oil
-
stimulates
-
Bovine serum albumin
-
slightly increases ACO activity, maximum value of ACO acitvity at 0.036 mM
-
casein
O74935
stimulates
di-(2-ethylhexyl)phthalate
-
-
fish oil
-
markedly increases enzyme activity
-
growth hormone
-
increases the mRNA of acyl CoA oxidase, directly induces the expression of AOX in adipocytes through STAT5A binding to the -1841 to -1825 site within the AOX promoter
-
jasmonate
Q5VRH3, Q69XR7
upregulates expression of ACX1, starts 4 h after treatment and remains elevated until 24 h
leptin
-
3fold increased activity at 100 ng/ml acute treatment
-
n-Alkane
-
increases ACO activity progressively with palmitoyl-CoA by 23%, with stearoyl-CoA by 42%, with behenoyl-CoA by 47% and with lignoceroyl-CoA by 75%
-
perilla oil
-
elevates AOX activity in a 4-day fedding, the effect is gradually decreased in a 4-week feeding
-
Peroxidase
-
stimulates, maximum value of ACO acitvity at 0.24 mg
-
Phenol
-
low concentration, magnitude of activation depends on the nature of the acyl-CoA substrate
prolactin
-
increases the mRNA of acyl CoA oxidase
-
Propionate
-
increase in propionate concentration lead to increase of enzyme amount
tetracosane
-
stimulates, highest activity with lignoceroyl-CoA as substrate
Triton X-100
-
stimulates, maximum value of ACO acitvity at 0.08%
MnCl2
-
slightly activating
additional information
Q5VRH3, Q69XR7
no upregulation by jasmonate; no upregulation by jasmonate
-
additional information
-
AOX stimulation is highly associated with the content of long chain n-3 polyunsaturated fatty acids
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0335
arachidoyl-CoA
-
-
0.032
Butyryl-CoA
-
-
0.1319
Butyryl-CoA
-
-
0.044
cis-3-decenoyl-CoA
-
mutant E421D
0.054
cis-3-decenoyl-CoA
-
wild-type
0.063
cis-3-hexenoyl-CoA
-
wild-type
0.076
cis-3-hexenoyl-CoA
-
mutant E421D
0.054
cis-3-Octenoyl-CoA
-
mutant E421D
0.057
cis-3-Octenoyl-CoA
-
wild-type
0.0093
Dec-4-cis-enoyl-CoA
-
-
0.002
decanoyl-CoA
-
recombinant enzyme
0.0072
decanoyl-CoA
O74935
30C
0.02
decanoyl-CoA
-
-
0.024
decanoyl-CoA
-
-
0.002
Dodecanoyl-CoA
-
MCOX
0.0157
Dodecanoyl-CoA
P0CZ23
isozyme AtACX3
0.0189
Dodecanoyl-CoA
P0CZ23
isozyme AtACX1
0.025
Dodecanoyl-CoA
-
pH 7.0-9.5
0.071
Dodecanoyl-CoA
-
pH 6.2
0.1
Dodecanoyl-CoA
O74935
30C
0.00633
Hexadecanedioyl-CoA
O74935
30C
0.006
Hexanoyl-CoA
-
isozyme SCOX
0.02
Hexanoyl-CoA
P0CZ23
isozyme AtSACX
0.03
Hexanoyl-CoA
-
in 50 mM phosphate buffer, pH 7.4, at 30C
0.067
Hexanoyl-CoA
-
recombinant enzyme
0.092
Hexanoyl-CoA
-
-
0.013
Lauroyl-CoA
-
-
0.024
Lauroyl-CoA
-
-
0.027
Lauroyl-CoA
-
liver enzyme
0.0025
lignoceroyl-CoA
-
-
0.0073
linoleoyl-CoA
-
-
0.0053
myristoyl-CoA
-
isozyme AtACX1
0.011
myristoyl-CoA
-
-
0.011
myristoyl-CoA
-
-
0.0116
myristoyl-CoA
-
-
0.029
myristoyl-CoA
-
-
0.005
O2
-
-
0.042
Octanoyl-CoA
-
-
0.0443
Octanoyl-CoA
-
pH 7.4, 30C, wild-type enzyme
0.0546
Octanoyl-CoA
-
pH 7.4, 30C, mutant enzyme E421D
0.058
Octanoyl-CoA
-
-
0.061
Octanoyl-CoA
-
-
0.087
Octanoyl-CoA
-
liver enzyme
0.011
oleoyl-CoA
-
-
0.046
oleoyl-CoA
-
-
0.00000002
palmitoyl-CoA
Q33DR0
-
0.00181
palmitoyl-CoA
-
kidney enzyme
0.007
palmitoyl-CoA
-
liver enzyme
0.01
palmitoyl-CoA
-
recombinant enzyme from Spodoptera frugiperda cells
0.0116
palmitoyl-CoA
-
-
0.02
palmitoyl-CoA
-
-
0.028
palmitoyl-CoA
Q8HYL8
AOX1
0.038
palmitoyl-CoA
Q8HYL8
AOX2
0.073
palmitoyl-CoA
-
isoform ACOX1a
0.09
palmitoyl-CoA
-
isoform ACOX1b
0.0044
stearoyl-CoA
-
isozyme AtACX2
0.0096
stearoyl-CoA
-
-
0.023
stearoyl-CoA
-
-
0.034
stearoyl-CoA
-
-
0.018
tetradecanoyl-CoA
O74935
30C
0.056
trans-3-decenoyl-CoA
-
wild-type
0.064
trans-3-decenoyl-CoA
-
mutant E421D
0.063
trans-3-hexenoyl-CoA
-
wild-type
0.083
trans-3-hexenoyl-CoA
-
mutant E421D
0.059
trans-3-octenoyl-CoA
-
wild-type
0.066
trans-3-octenoyl-CoA
-
mutant E421D
0.019
linoleoyl-CoA
-
-
additional information
additional information
-
overview: Km of several monocarboxylic and dicarboxylic acyl-CoA as substrates
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.225
Butyryl-CoA
-
-
0.04
cis-3-decenoyl-CoA
-
mutant E421D
0.06167
cis-3-decenoyl-CoA
-
wild-type
0.165
cis-3-hexenoyl-CoA
-
mutant E421D
0.35
cis-3-hexenoyl-CoA
-
wild-type
0.053
cis-3-Octenoyl-CoA
-
mutant E421D
0.075
cis-3-Octenoyl-CoA
-
wild-type
1.53
decanoyl-CoA
-
recombinant enzyme
0.089
Hexanoyl-CoA
-
in 50 mM phosphate buffer, pH 7.4, at 30C
0.203
Hexanoyl-CoA
-
-
0.07
Octanoyl-CoA
-
-
2.18
Octanoyl-CoA
-
pH 7.4, 30C, mutant enzyme E421D
3.47
Octanoyl-CoA
-
pH 7.4, 30C, wild-type enzyme
78
palmitoyl-CoA
Q33DR0
-
0.0053
trans-3-decenoyl-CoA
-
mutant E421D
0.01567
trans-3-decenoyl-CoA
-
wild-type
0.0283
trans-3-hexenoyl-CoA
-
mutant E421D
0.05
trans-3-hexenoyl-CoA
-
wild-type
0.012
trans-3-octenoyl-CoA
-
mutant E421D
0.045
trans-3-octenoyl-CoA
-
wild-type
8.59
Hexanoyl-CoA
-
recombinant enzyme
additional information
additional information
-
pH-dependency of turnover number
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00047
3-ketohexadecanoyl-CoA
-
-
0.3
acetyl-CoA
-
-
0.03
CoA
-
low concentration
0.32
CoA
-
high concentration
0.55
FMN
-
-
0.045
oct-2-en-4-ynoyl-CoA
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000016
-
activity in one peroxisomal acyl-coenzyme A oxidase deficiency patient, pH not specified in the publication, temperature not specified in the publication
0.0006
-
liver homogenate
0.00502
-
glucose-grown cultures with stearoyl-CoA as substrate
0.00571
-
glucose-grown cultures with behenoyl-CoA as substrate
0.00613
-
glucose-grown cultures with palmitoyl-CoA as substrate
0.00615
-
glucose-grown cultures with lignoceroyl-CoA as substrate
0.00714
-
alkane-grown cultures with stearoyl-CoA as substrate
0.00758
-
alkane-grown cultures with palmitoyl-CoA as substrate
0.008 - 4
-
alkane-grown cultures with behenoyl-CoA as substrate
0.0108
-
alkane-grown cultures with lignoceroyl-CoA as substrate
0.375
-
purified isozyme SCOX
1.7
Q33DR0
crude enzyme; crude extract, at 37C
1.95
-
recombinant enzyme, purified
2.04
-
purified enzyme
2.12
-
purified enzyme
5.3
-
highly purified isozyme MCOX
19.7
O74935
-
27
-
purified enzyme
27.2
-
purified enzyme
58
-
purified enzyme
60.9
Q33DR0
purified enzyme; purified recombinant enzyme, at 37C
77.14
-
purified enzyme
additional information
-
overview: specific activity of enzyme from several sources with several substrates
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
isoform ACOX1a exhibits only 50% specific activity toward palmitoyl-CoA as compared to ACOX1b; specific activities in units/mg for isoform ACOX1a: 0.186 for eicosapentaenoyl-CoA, 0.237 for 4-methyl-nonanoyl-CoA, 0.15 for 16-hydroxy-palmitoyl-CoA, 0.336 for 4,8,12-trimethyl-tridecanoyl-CoA, 0.372 for 1,16-hexadecadioyl-CoA, 0.699 for 6-phenyl-6-phenyl-hexanoyl-CoA, 0.076 for palmitoyl-CoA, specific activities in units/mg for isoform ACOX1b: 0.226 for eicosapentaenoyl-CoA, 0.278 for 4-methyl-nonanoyl-CoA, 0.298 for 16-hydroxy-palmitoyl-CoA, 0.423 for 4,8,12-trimethyl-tridecanoyl-CoA, 0.504 for 1,16-hexadecadioyl-CoA, 0.573 for 6-phenyl-6-phenyl-hexanoyl-CoA, 0.166 for palmitoyl-CoA
additional information
-
no activity in a second peroxisomal acyl-coenzyme A oxidase deficiency patient
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
-
recombinant enzyme
7.5 - 8.5
-
optimal palmitoyl-CoA oxidase activity for ACOX1b
8.3 - 8.5
-
-
8.3 - 8.6
-
isozyme SCOX
8.5
-
optimal palmitoyl-CoA oxidase activity for ACOX1a
8.6
-
isozyme MCOX
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
-
pH 7: about 30% of activity maximum, pH 10: about 5% of activity maximum, inactive below pH 6.5
7.2 - 9.3
-
both isoforms
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28 - 38
-
recombinant enzyme
37
-
assay at
37.5
-
the ACOX1b isoform has a maximum specific activity around 37.5C
40
-
the maximum specific activity for ACOX1a is obtained at 40C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 55
-
recombinant enzyme, at 5C, 21% activity, at 55C, 78% activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q4QRE2
discreetly expressed, lower levels of transcript variant ACOX1-3I, the ACOX1-3I transcript variant is expressed seven times less in brain than the ACOX1-3II variant
Manually annotated by BRENDA team
Q4QRE2
discreetly expressed, lower levels of transcript variant ACOX13II, the ACOX13II transcript variant is expressed seven times more in brain than the ACOX13I variant
Manually annotated by BRENDA team
-
developing, germinating
Manually annotated by BRENDA team
-
acox1 transcripts diffusely distributed in early-stage embryonic cells
Manually annotated by BRENDA team
-
significant pretranslational up-regulation of acox1 expression in the anterior intestine after feeding
Manually annotated by BRENDA team
Q4QRE2
widely present at later stages, high levels of transcript variant ACOX13II in the anterior intestine, significant pretranslational up-regulation of acox1 expression in the anterior intestine after feeding
Manually annotated by BRENDA team
Q4QRE2
widely present at later stages, high levels of transcript variants ACOX1-3I in the anterior intestine, significant pretranslational up-regulation of acox1 expression in the anterior intestine after feeding
Manually annotated by BRENDA team
Q4QRE2
widely present at later stages, high levels of transcript variant ACOX1-3I
Manually annotated by BRENDA team
Q4QRE2
widely present at later stages, high levels of transcript variant ACOX13II
Manually annotated by BRENDA team
-
before anthesis
Manually annotated by BRENDA team
Cucurbita sp.
-
-
Manually annotated by BRENDA team
Q5VRH3, Q69XR7
ACX1 barely detectable
Manually annotated by BRENDA team
Q5VRH3, Q69XR7
ACX3 expression less prominent compared to ACX2
Manually annotated by BRENDA team
Q5VRH3, Q69XR7
predominant expression of ACX2
Manually annotated by BRENDA team
-
low content
Manually annotated by BRENDA team
additional information
-
always present along the barley life cycle, while a higher level of expression is typical of actively growing tissues such as germinating embryos, ovary before anthesis, developing embryos, shoots and root apexes
Manually annotated by BRENDA team
additional information
-
SK32 cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Cucurbita sp.
-
-
Manually annotated by BRENDA team
-
existence of two independent, Pex5p-mediated import pathways into peroxisomes in yeast: 1. a classical peroxisomal targeting signal 1 pathway and a novel, non-PTS1 pathway for Pox1p
Manually annotated by BRENDA team
Sporidiobolus ruineniae CBS5001, Arabidopsis thaliana Col-0
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
-
SDS-PAGE
685352
60000
-
isoform SCOX, gel filtration
391069
62000
-
isoform MCOX, gel filtration
391069
72000
-
Western blot analysis
673774
76400
Q33DR1
predicted
672429
76500
Q33DR0
predicted from amino acid sequence
672429
81000
-
isoform ACOX1a and ACOX1b, SDS-PAGE
684861
100000
-
gel filtration
391060
136000
-
gel filtration
391045
139000
-
sedimentation equilibrium method
391043
139000
-
noninducible trihydroxycoprostanoyl-CoA oxidase
391048
140000
-
native AtACX1 and AtACX2, and recombinant AtACX1, gel filtration
391070
145000
-
inducible fatty acyl-CoA oxidase, gel filtration
391048
150000
-
gel filtration
391059
150000
O65201, O65202, P0CZ23, Q96329, Q9ZQP2
-
689649
160000
Q33DR0
native-PAGE
672429
180000
Q33DR0
SDS-PAGE, recombinant enzyme
672429
188000
O65201, O65202, P0CZ23, Q96329, Q9ZQP2
ACX4
689649
190000
Q33DR0
gel filtration; gel filtration, recombinant enzyme
672429
427000
-
noninducible fatty acyl-CoA oxidase, gel filtration
391048
552000
-
ultracentrifugation
391052
600000
-
sedimentation equilibrium
391050
660000
-
recombinant AtACX2, aggregation in E. coli, gel filtration
391070
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 72000, SDS-PAGE
?
-
? * 15000, isoform SCOX, labile multimeric structure, SDS-PAGE
?
-
? * 51000 + ? * 21000, recombinant enzyme, SDS-PAGE
?
Cucurbita sp.
-
? * 73000, SDS-PAGE and sequence determination
?
-
? * 52000 + ? * 22500, liver, SDS-PAGE, inducible fatty acyl-CoA oxidase
?
Q33DR0
x * 76500, SDS-PAGE
?
Arthrobacter ureafaciens NBRC 12140
-
x * 76500, SDS-PAGE
-
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 72000, SDS-PAGE
dimer
-
2 * 71000, liver, SDS-PAGE, noninducible fatty acyl-CoA oxidase
dimer
-
2 * 74300, AtACX1 and AtACX2, sequence determination
hexamer
-
6 * 69000, liver, SDS-PAGE, noninducible trihydroxyprostanoyl-CoA oxidase
homodimer
Q33DR0
2 * 75000, SDS-PAGE
homodimer
-
2 * 75000
homodimer
Q33DR0
2 * 95000, gel filtration
homodimer
Arthrobacter ureafaciens NBRC 12140
-
2 * 75000, SDS-PAGE, 2 * 95000, gel filtration
-
homotetramer
O65201, O65202, P0CZ23, Q96329, Q9ZQP2
4 * 47000, ACX4
monomer
-
1 * 62000, isoform MCOX, SDS-PAGE
octamer
-
8 * 75000, SDS-PAGE
octamer
-
8 * 72100, SDS-PAGE
tetramer
-
2 * 45000 + 2 * 22000, SDS-PAGE
tetramer
-
crystallographic studies
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by the hanging drop vapor diffusion technique, ACX4-acetoacetyl-CoA crystals to 2.7 A resolution, of His-tagged ACX4 to 3.9 A resolution
-
hanging-drop vapor-diffusion method, crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions, a = 85.6 A, b = 117.0 A, c = 1313.3 A
-
hanging-drop vapour-diffusion method, the crystals diffract to 2.0 A using synchrotron radiation, have unit-cell parameters a = 85.2, b = 118.0, c = 131.0 A, alpha = beta = gamma = 90 and show P2(1)2(1)2(1) symmetry
-
at 5C from a 30% saturated ammonium sulfate solution, yellow rod-shaped crystals
-
cocrystallization of ACO-II with lauroyl-CoA by the hanging-drop vapor-diffusion method under oil, to 2.07 A resolution
P07872
native ACO-II, hanging-drop vapor-diffusion method with 3% (w/v) polyethylene glycol 20000 as precipitant in 20 mM potassium phosphate, pH 7.4; X-ray structure analysis
-
to 2.74 A resolution by vapor diffusion hanging-drop method, unusual packing arrangement of the tomato AXC1 enzyme as compared to other ACX enzymes, three monomers of ACX1 are present in the asymmetric unit
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9
-
35C, 60 min
391050
6.5 - 7.5
Q33DR0
at 37C
672429
7 - 9
-
stable for 120 min
674349
additional information
Q33DR0
between 6.57.5 at 37C
672429
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 40
-
stable for 120 min
674349
37.5 - 70
-
the ACOX1b isoform retains 57% of its specific activity at 50C and is more resistant to heat denaturation than ACOX1a since it conserves 30% of its specific activity after treatment at 50C, the isoform shows 70% specific activity at 37.5C
684861
50
-
10 min
391050
50
-
the specific activity of isoform ACOX1a drops to zero at 50C
684861
60
-
30 min, with butyryl-CoA and FAD, 50% loss of activity; 30 min, with butyryl-CoA, without FAD, 85% loss of activity
391060
65
-
10 min, complete inactivation
391050
additional information
-
FAD enhances thermal stability
391060
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis, 4C, 24 h, 80% loss of activity
-
stabilization with benzoate necessary for purification of the holoenzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, potassium phosphate buffer, pH 7.0
Q33DR0
37C, 0.2 M potassium phosphate (pH 7.5) containing 0.1 M FAD, 4 h, less than 10% loss of activity
Q33DR0
-20C, 25% glycerol, 8 months
-
-20C, pH 7.4, 2 months
-
4C, pH 7.4, 2 months, 20% loss of activity
-
frozen, 10% sucrose, several weeks
-
-20C, for at least 1 month
-
-80C, wild-type enzyme and mutant enzymes E421D, E421A, E421Q and E421G are stable for 3 months
-
4C, His-tagged enzyme is stable for 1 week
-
-30C, 35% glycerol (v/v), at least 1 month
-
-30C, in presence of 35% v/v glycerol, stable for at least 1 year
O74935
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by gel filtration and anion exchange chromatography
-
recombinant from Escherichia coli
P0CZ23
by gel filtration; Q-Sepharose column chromatography and CM-Sepharose column chromatography
Q33DR0
partially
Cucurbita sp.
-
Ni-NTA column chromatography
-
partially
-
recombinant His-tagged from Spodoptera frugiperda cells
-
ACO-i and ACO-II, recombinant from Escherichia coli
-
holo- and apoenzyme
-
native and recombinant ACO-II from Escherichia coli
-
nickel metal-affinity resin column chromatography
-
to homogeneity
-
recombinant from Escherichia coli, His-tagged
-
both isoforms
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL 21
-
expression in Escherichia coli of His-tagged proteins: AtSACX, AtACX1, and AtACX3, sequence analysis also with AtACX2
P0CZ23
expression of AtACX1 and AtACX2 in Escherichia coli; plant anti-sense constructs, investigation of substrate specificities and regulation
-
into the pET24 vector and transformed into Escherichia coli BL21(DE3)
-
into vector pUTE300, expression in Escherichia coli JM109
Q33DR1
expressed in Escherichia coli JM109 cells; into vector pUTE300, expression in Escherichia coli JM109
Q33DR0
gene aoxA, seuence comparisons, recombinant expression from plasmid in Aspergillus nidulans strain MH11036, complementation of enzyme deficient aoxADELTA strain MH11074, expression as GFP-tagged enzyme showing PexE-dependent peroxisomal localisation
-
sequence analysis
-
expression in Escherichia coli
-
transformed SK32 cells stably expressing one of the wild type Pex5p isoforms, Pex5pM and S restore the processing of Aox, but Pex5pL does not
-
sequence analysis
Cucurbita sp.
-
expression in Escherichia coli of 2 genes: ACX1.1 and ACX1.2, sequence comparison with other species
-
expressed in Escherichia coli strains BL21 and C41, and in COS-7 cells (His-tagged enzyme)
-
expression as His-tagged protein in Spodoptera frugiperda cells via infection with Baculovirus
-
expression of human ACOX1b isoform in a mouse ACOX1b mutant can reverse the null phenotype, overview
-
SCOX expression analysis in peroxisomal acyl-coenzyme A oxidase deficiency patients, overview
-
overexpression in Escherichia coli
-
sequence analysis, expression analysis during development
-
expression in COS-7 cells
Q8HYL8
ACO-I and ACO-II; expression in Escherichia coli
-
cloned into a bacterial expression vector pLM1 with six continous His codons attached to the 5' end of the gene, overexpression of wild-type ands mutant enzymes E421D, E421A, E421Q and E421G in Escherichia coli
-
expressed in Escherichia coli
P07872
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
His-tagged
-
into vector pTZ18R
-
sequence analysis and regulation
-
expression in Escherichia coli as an active, N-terminal tagged His6 fusion protein
O74935
expression of His-tagged enzyme in Escherichia coli
-
genes POX1-POX6, heterologous co-expression of the different isozymes with polyhydroxyalkanoate synthase (phaC) of Pseudomonas aeruginosa in Yarrowia lipolytica strains, subcloning in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C159T
Q33DR0
exhibits 60% activity of the wild-type enzyme, looses more than half of the activity after incubation with N-ethylmaleimide
C159T
Q33DR0
60% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide
C159T/C420S
Q33DR0
activity less than one tenth of that of the wild type
C159T/C420S/C424V
Q33DR0
shows no activity at all
C159T/C424V
Q33DR0
activity less than one tenth of that of the wild type
C420S
Q33DR0
exhibits 41% activity of the wild-type enzyme, retains about 90% of the activity after incubation with N-ethylmaleimide
C420S
Q33DR0
41% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide
C420S/424V
Q33DR0
activity less than one tenth of that of the wild type
C424V
Q33DR0
looses more than half of the activity after incubation with N-Ethylmaleimide
C424V
Q33DR0
98% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide
C159T
Arthrobacter ureafaciens NBRC 12140
-
exhibits 60% activity of the wild-type enzyme, looses more than half of the activity after incubation with N-ethylmaleimide, 60% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide
-
C420S
Arthrobacter ureafaciens NBRC 12140
-
exhibits 41% activity of the wild-type enzyme, retains about 90% of the activity after incubation with N-ethylmaleimide, 41% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide
-
C424V
Arthrobacter ureafaciens NBRC 12140
-
looses more than half of the activity after incubation with N-Ethylmaleimide
-
G432R
-
conversion of Aox from component A to components B and C is completely prevented at both 30C and 37C
G231V
Q15067
the mutation in combination with skipping of exon 13 leads to peroxisomal acyl-CoA oxidase deficiency
E421A
-
inactive mutant enzyme
E421A
-
does not show any isomerase activity
E421D
-
Km-value for octanoyl-CoA is 1.23fold higher than the wild-type value. The turnover number for octanoyl-CoA is 1.6fold lower than activity of the wild-type enzyme
E421D
-
isomerase activity is decreased for all tested cis- and trans-substrates compared with that of wild-type enzyme
E421G
-
inactive mutant enzyme
E421Q
-
inactive mutant enzyme
T138I
-
compromised in wound-response signaling owing to a deficiency in jasmonic acid synthesis, FAD is not bound in the mutant protein
additional information
O65201, P0CZ23
acx1-1 mutant, acx1-1 acx2-1 double mutant, lipid catabolism during germination and early post-germinative growth is unaltered in the acx1-1 mutant, seedlings of the double mutant acx1-1 acx2-1 are unable to catabolize seed storage lipid, accumulate long-chain acyl-CoAs, and are unable to establish photosynthetic competency in the absence of an exogenous carbon supply, germination frequency of the double mutant acx1-1 acx2-1 is significantly reduced compared with wild-type seeds, is improved by dormancy-breaking treatments, the acx1-1 and acx1-2 acx2-1 double mutants exhibit a sucrose-independent germination phenotype, wound-induced increase in jasmonic acid is only compromised in the acx1-1 mutant
additional information
O65201, P0CZ23
acx2-1 mutant, acx1-1 acx2-1 double mutant, lipid catabolism during germination and early post-germinative growth is slightly delayed in the acx2-1 mutant, with 3-day-old acx2-1 seedlings accumulating long-chain acyl-CoAs, seedlings of the double mutant acx1-1 acx2-1 are unable to catabolize seed storage lipid, accumulate long-chain acyl-CoAs, and are unable to establish photosynthetic competency in the absence of an exogenous carbon supply, germination frequency of the double mutant acx1-1 acx2-1 is significantly reduced compared with wild-type seeds, is improved by dormancy-breaking treatments, the acx2-1 and acx1-2 acx2-1 double mutants exhibit a sucrose-independent germination phenotype
additional information
-
mutants defective in ACX1, ACX3, or ACX4 have reduced fatty acyl-CoA oxidase activity, acx1 acx2 double mutants display enhanced indole-3-butyric acid resistance and are sucrose dependent during seedling development, acx1 acx3 and acx1 acx5 double mutants display enhanced indole-3-butyric acid resistance but remain sucrose independent
additional information
-
the ibr3-1 acx3-4 double mutant shows greatly enhanced indole-3-butyric acid resistance
additional information
-
generation of higher-order acx mutants, the acx3acx4Col and acx1acx3acx4Col mutants are viable, enzyme activity in these mutants is significantly reduced on a range of substrates compared to the wild-type
additional information
Arabidopsis thaliana Col-0
-
generation of higher-order acx mutants, the acx3acx4Col and acx1acx3acx4Col mutants are viable, enzyme activity in these mutants is significantly reduced on a range of substrates compared to the wild-type
-
R210H
-
naturally occuring apparent homozygous missense mutation c.629G/A of SCOX in a peroxisomal acyl-coenzyme A oxidase deficiency patient
additional information
-
ACOX1-/- mice show twofold increased expression of isozyme ACOX1a compared to wild-type mice, ACOX1b-/- and ACOX1a-/- phenotypes, overview. Expression of human ACOX1b isoform in a mouse ACOX1b mutant can reverse the hepatic null phenotype, but with only weak reversal of the hepatic steatosis phenotype in the mice, overview. Expression of human isozyme ACOX1a has only poor effects
E421Q
-
does not show any isomerase activity
additional information
-
OAF1-gene disrupted construct with reduced number of peroxisomes, no longer inducible by oleate
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
Q33DR0
useful for the determination of free fatty acids
analysis
Arthrobacter ureafaciens NBRC 12140
-
useful for the determination of free fatty acids
-
degradation
-
ACO activity in Beauveria bassiana depends on the carbon source used for growth and the chain length of the substrate utilized for the oxidation reaction
degradation
Beauveria bassiana GHA
-
ACO activity in Beauveria bassiana depends on the carbon source used for growth and the chain length of the substrate utilized for the oxidation reaction
-
biotechnology
-
potential depolluting agent by degradation of oils, several biotechnological applications: production of metabolites, such as citrate, secretion of proteins, degradation of fatty acids
analysis
-
amperometric propionate sensor
additional information
-
inability of ACX1, ACX3, and ACX4 to fully compensate for one another in indole-3-butyric acid-mediated root elongation inhibition and ability of ACX2 and ACX5 to contribute to indole-3-butyric acid response suggests that indole-3-butyric acid-response defects in acx mutants may reflect indirect blocks in peroxisomal metabolism and indole-3-butyric acid beta-oxidation, rather than direct enzymatic activity of ACX isozymes on indole-3-butyric acid-CoA
additional information
-
solvent-accessible acyl binding pocket is not required for oxygen reactivity, the oligomeric state plays a role in substrate pocket architecture but is not linked to oxygen reactivity
nutrition
-
engineering of plants with increased content of monocarboxylic fatty acids in this essential oil crop by enzyme overexpression
additional information
-
novel Pex5pM is functional and a seven amino acids-insertion, which is present in the L isoform but absent in the M isoform, plays some role in the process of maturation of Aox
additional information
-
ACOX1 alternative splicing isoforms play a key conserved role in the vertebrate fatty acid metabolism, tissue-specific modulation of ACOX1 activity by exchanging exon 3 duplicated isoforms containing amino acid sequences that are potentially implicated in fatty acyl chain specificity
medicine
-
ACOX1 is a rate-limiting enzyme in peroxisomal fatty acids beta-oxidation and its deficiency is associated with a lethal, autosomal recessive disease, called pseudoneonatal-adrenoleukodystrophy
additional information
Q5VRH3, Q69XR7
three distinct ACX genes, ACX1 is upregulated by wounding, both locally and systemically, ACX1 may play a role in the synthesis of jasmonic acid in response to wounding
additional information
Q5VRH3, Q69XR7
three distinct ACX genes, expression of ACX2 remains unchanged by wounding, ACX2 may be involved in providing germinating seeds with sugar and energy
additional information
Q5VRH3, Q69XR7
three distinct ACX genes, expression of ACX3 remains unchanged by wounding
medicine
-
AOX activity is negatively correlated with postprandial triacylglycerol levels
additional information
-
isomerase activity of rat peroxisomal acyl-CoA oxidase I, is probably due to a spontaneous process driven by thermodynamic equilibrium with formation of a conjugated structure after deprotonation of substrate alpha-proton
additional information
-
nervonic acid is discharged from the spore into the external medium during firing along with the catalase and ACOX enzymes